Abstract
Collagen, the most abundant protein in mammals, has been widely used in biomedical materials. In order to increase the structural stability of collagen, we designed and synthesized the collagen mimetic peptides (CMPs) in which an oligopeptide with a high self-assembly propensity was attached. By this design, we expected that the oligopeptide could stabilize the collagen triple helix and assist their self-assembly into higher order structures. Since some of the CMPs containing Ab(16-22) sequence showed the ability to inhibit the aggregation of A protein in our previous studies, in the first part of this study, we further investigated their cytotoxicity by MTT assay. The results indicate that these CMPs are actually toxic to a Neuro cell N2a. Therefore, in the second part, we chose another oligopeptide CILFWG as an attachment to CMPs. From this design, we synthesized a series of CMPs : CILFWG(POG)7, (POG)7CILFWG, and OG(POG)4CILFWG. The collagen peptide (POG)7 and CILFWG peptide were also synthesized for comparison. We used UV-VIS spectroscopy, TEM, and CD to characterize these peptides. The results showed that the oligopeptide could stabilize the collagen triple helices and assist their self-assembly into higher order structures. In particular, this oligopeptide has a more pronounced effect on CILFWG(POG)7 than any other peptide studied. Thus, this oligopeptide could be potentially useful in designing stable collagen assemblies and related biomaterials.